This project concerns the biochemical and genetic studies of murein metabolism in E. coli. It is generally assumed that the biosynthesis, degradation and remodeling of the rigid layer of the E. coli cell envelope plays an important role in the control and execution of cell division in E. coli. Work in progress includes the purification of murein hydrolases from E. coli and the isolation and characterization of mutants with altered murein hydrolase activities. We are also investigating the biosynthesis of a unique lipoprotein which is covalently attached to the murein. BIBLIOGRAPHIC REFERENCES: (i) Yem, D. and H.C. Wu, 1976, Purification and properties of beta-N-acetylglucosaminidase from E.coli K-12. J. Bacteriol. 125: 324-331. (ii) Yem, D. and H.C. Wu, 1976. Isolation of Escherichia coli mutants with altered levels of beta-N-acetylglucosaminidase. J. Bacteriol. 125: 372-373.